| Autor: |
Iurchenko VS, Illarionova NG, Denisov IG, Ponomareva RB, Rozhetskaia KM |
| Jazyk: |
ruština |
| Zdroj: |
Prikladnaia biokhimiia i mikrobiologiia [Prikl Biokhim Mikrobiol] 1989 Jan-Feb; Vol. 25 (1), pp. 15-21. |
| Abstrakt: |
The enzymatic and conformational stability of Bacillus subtilis alpha-amylase and its polymeric complexes in acid media and subsequent renaturation in weakly alkaline media were investigated. The following parameters of alpha-amylase secondary structure were determined from circular dichroism spectra: helical units -25%, beta-structures -9%; beta-turns -13%; disordered conformations -53%. After complexation with polymethacrylic acid (PMAA) the alpha-amylase secondary structure did not change, and the tertiary structure underwent only small local changes. Complexation of alpha-amylase with linear and cross-linked PMAA led to an increase in both enzymatic and conformational stabilities in acid media. Purification of alpha-amylase using a biosorbent resulted in higher acid resistance of the free enzyme and of that in the complex with PMAA. Moreover, the degree of reversibility of the acid inactivation also increased. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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